Additionally, denaturation of IDP homogenizes their disordered structure. In such cases, the IDP segments, regardless of their sequence, have a very similar structural scaling to chemically unfolded structured protein (\(R_g=1.927 N^{0.598}\)  Å) [1]}. On average, our SAXS measurements at 3M GdnHcl show a scaling behaviour of \(R_g=(1.99 \pm 0.06) N^{0.61\pm 0.02}\)  Å. We emphasize that both trFRET and SAXS show expansion with denaturing, which is consistent with recent works [2]}.
